ID   NIRB_ECOLI              Reviewed;         847 AA.
AC   P08201; Q2M731;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 4.
DT   16-JUN-2009, entry version 90.
DE   RecName: Full=Nitrite reductase [NAD(P)H] large subunit;
DE            EC=1.7.1.4;
GN   Name=nirB; OrderedLocusNames=b3365, JW3328;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=89282391; PubMed=2543955; DOI=10.1093/nar/17.10.3865;
RA   Bell A.I., Gaston K.L., Cole J.A., Busby S.J.W.;
RT   "Cloning of binding sequences for the Escherichia coli transcription
RT   activators, FNR and CRP: location of bases involved in discrimination
RT   between FNR and CRP.";
RL   Nucleic Acids Res. 17:3865-3874(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=90345936; PubMed=2200672;
RX   DOI=10.1111/j.1432-1033.1990.tb19125.x;
RA   Peakman T., Crouzet J., Mayaux J.F., Busby S.J.W., Mohan S.,
RA   Harborne N., Wootton J., Nicolson R., Cole J.A.;
RT   "Nucleotide sequence, organisation and structural analysis of the
RT   products of genes in the nirB-cysG region of the Escherichia coli K-12
RT   chromosome.";
RL   Eur. J. Biochem. 191:315-323(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-21.
RX   MEDLINE=88062713; PubMed=2445993; DOI=10.1016/0022-2836(87)90404-9;
RA   Jayaraman P.S., Peakman T.C., Busby S.J.W., Quincey R.V., Cole J.A.;
RT   "Location and sequence of the promoter of the gene for the NADH-
RT   dependent nitrite reductase of Escherichia coli and its regulation by
RT   oxygen, the Fnr protein and nitrite.";
RL   J. Mol. Biol. 196:781-788(1987).
CC   -!- CATALYTIC ACTIVITY: Ammonium hydroxide + 3 NAD(P)(+) + H(2)O =
CC       nitrite + 3 NAD(P)H.
CC   -!- COFACTOR: Binds 1 siroheme per subunit.
CC   -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit.
CC   -!- COFACTOR: FAD.
CC   -!- PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation).
CC   -!- SUBUNIT: Homodimer which associates with nirD.
CC   -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S
CC       domain family.
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DR   EMBL; X14202; CAA32416.1; -; Genomic_DNA.
DR   EMBL; U18997; AAA58162.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76390.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77925.1; -; Genomic_DNA.
DR   PIR; H65130; H65130.
DR   RefSeq; AP_004424.1; -.
DR   RefSeq; NP_417824.1; -.
DR   GeneID; 947868; -.
DR   GenomeReviews; AP009048_GR; JW3328.
DR   GenomeReviews; U00096_GR; b3365.
DR   KEGG; ecj:JW3328; -.
DR   KEGG; eco:b3365; -.
DR   EchoBASE; EB0647; -.
DR   EcoGene; EG10653; nirB.
DR   HOGENOM; P08201; -.
DR   OMA; P08201; NIQRNGT.
DR   BioCyc; EcoCyc:NIRB-MON; -.
DR   BioCyc; MetaCyc:NIRB-MON; -.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0009055; F:electron carrier activity; IEA:InterPro.
DR   GO; GO:0050660; F:FAD binding; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0050661; F:NADP or NADPH binding; IEA:InterPro.
DR   GO; GO:0008942; F:nitrite reductase [NAD(P)H] activity; IEA:EC.
DR   GO; GO:0042128; P:nitrate assimilation; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR007419; BFD_Fer2_bd.
DR   InterPro; IPR013027; FAD_pyr_nucl-diS_OxRdtase.
DR   InterPro; IPR006066; Nir_Si_BS.
DR   InterPro; IPR006067; Nir_Sir_4Fe4S.
DR   InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer.
DR   InterPro; IPR012744; Nitri_red_NirB.
DR   InterPro; IPR017121; Nitrite_Rdtase_lsu.
DR   InterPro; IPR001327; Pyr_OxRdtase_NAD_bd.
DR   Pfam; PF04324; Fer2_BFD; 1.
DR   Pfam; PF01077; NIR_SIR; 1.
DR   Pfam; PF03460; NIR_SIR_ferr; 1.
DR   Pfam; PF00070; Pyr_redox; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PIRSF; PIRSF037149; NirB; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00397; SIROHAEM.
DR   ProDom; PD000139; FAD_pyr_redox; 1.
DR   TIGRFAMs; TIGR02374; nitri_red_nirB; 1.
DR   PROSITE; PS00365; NIR_SIR; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Complete proteome; FAD; Flavoprotein; Heme; Iron; Iron-sulfur;
KW   Metal-binding; NADP; Nitrate assimilation; Oxidoreductase.
FT   CHAIN         1    847       Nitrite reductase [NAD(P)H] large
FT                                subunit.
FT                                /FTId=PRO_0000199962.
FT   NP_BIND      44     79       FAD (Potential).
FT   NP_BIND     193    225       NAD or NADP (Potential).
FT   METAL       641    641       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       647    647       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       681    681       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       685    685       Iron (siroheme axial ligand) (By
FT                                similarity).
FT   METAL       685    685       Iron-sulfur (4Fe-4S) (By similarity).
FT   CONFLICT    442    442       G -> A (in Ref. 1 and 2).
FT   CONFLICT    835    847       YERIPVTLVEDNA -> MNVSQ (in Ref. 1 and 2).
SQ   SEQUENCE   847 AA;  93121 MW;  5265AD93FD390EB4 CRC64;
     MSKVRLAIIG NGMVGHRFIE DLLDKSDAAN FDITVFCEEP RIAYDRVHLS SYFSHHTAEE
     LSLVREGFYE KHGIKVLVGE RAITINRQEK VIHSSAGRTV FYDKLIMATG SYPWIPPIKG
     SDTQDCFVYR TIEDLNAIES CARRSKRGAV VGGGLLGLEA AGALKNLGIE THVIEFAPML
     MAEQLDQMGG EQLRRKIESM GVRVHTSKNT LEIVQEGVEA RKTMRFADGS ELEVDFIVFS
     TGIRPRDKLA TQCGLDVAPR GGIVINDSCQ TSDPDIYAIG ECASWNNRVF GLVAPGYKMA
     QVAVDHILGS ENAFEGADLS AKLKLLGVDV GGIGDAHGRT PGARSYVYLD ESKEIYKRLI
     VSEDNKTLLG AVLVGDTSDY GNLLQLVLNA IELPENPDSL ILPAHSGSGK PSIGVDKLPD
     SAQICSCFDV TKGDLIAAIN KGCHTVAALK AETKAGTGCG GCIPLVTQVL NAELAKQGIE
     VNNNLCEHFA YSRQELFHLI RVEGIKTFEE LLAKHGKGYG CEVCKPTVGS LLASCWNEYI
     LKPEHTPLQD SNDNFLANIQ KDGTYSVIPR SPGGEITPEG LMAVGRIARE FNLYTKITGS
     QRLAMFGAQK DDLPEIWRQL IEAGFETGHA YAKALRMAKT CVGSTWCRYG VGDSVGLGVE
     LENRYKGIRT PHKMKFGVSG CTRECSEAQG KDVGIIATEK GWNLYVCGNG GMKPRHADLL
     AADIDRETLI KYLDRFMMFY IRTADKLTRT APWLENLEGG IDYLKAVIID DKLGLNAHLE
     EEMARLREAV LCEWTETVNT PSAQTRFKHF INSDKRDPNV QMVPEREQHR PATPYERIPV
     TLVEDNA
//